NDLI: Insights into the binding mode of curcumin to MD-2: studies from molecular docking, molecular dynamics simulations and experimental assessments.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wang, Zhe Chen, Gaozhi Chen, Linfeng Liu, Xing Fu, Weitao Zhang, Yali Li, Chenglong Liang, Guang Cai, Yuepiao
Description	Author Affiliation: Wang Z ( Chemical Biology Research Center, School of Pharmaceutical Sciences, Wenzhou Medical University, Wenzhou, Zhejiang 325035, China. ypcai@wmu.edu.cn wzmcliangguang@163.com.)
Abstract	Curcumin, a natural product, has been shown to possess notable anti-inflammatory activities and numerous studies have been carried out on its clinical applications. Recently, several reports mentioned that myeloid differentiation protein 2 (MD-2) may be the direct target of curcumin in the inhibition of lipopolysaccharide (LPS) signaling. However, the exact interaction between curcumin and MD-2 is still incompletely understood. In the present study, computational and experimental methods were employed to explore the underlying structural mechanism of curcumin binding to the MD-2 protein. Molecular docking and molecular dynamics (MD) simulation studies showed that curcumin could be embedded into the hydrophobic pocket of MD-2 and form stable hydrogen bonding interactions with residues R90 and Y102 of MD-2. Moreover, experimental results of curcumin binding to the MD-2(R90A/Y102A) mutant further confirmed that residues ARG-90 and TYR-102 contribute to the recognition process of curcumin binding to the MD-2 protein. In conclusion, we have explored the binding mechanism of curcumin to MD-2; more importantly, this work could offer useful references for designing novel analogs of curcumin as potential anti-inflammatory agents targeting the MD-2 protein.
File Format	HTM / HTML
ISSN	1742206X
Issue Number	7
Volume Number	11
e-ISSN	17422051
Journal	Molecular BioSystems
Language	English
Publisher	Royal Society of Chemistry
Publisher Date	2015-07-01
Publisher Place	Great Britain (UK)
Access Restriction	Subscribed
Subject Keyword	Discipline Molecular Biology Discipline Biochemistry Anti-inflammatory Agents, Non-steroidal Chemistry Curcumin Lymphocyte Antigen 96 Animals Binding Sites Cell Line Humans Hydrogen Bonding Hydrophobic And Hydrophilic Interactions Mice Molecular Docking Simulation Molecular Dynamics Simulation Protein Binding Thermodynamics Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

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